eF-site ID 5irx-B PDB Code 5irx Chain B click to enlarge Title Structure of TRPV1 in complex with DkTx and RTX, determined in lipid nanodisc Classification TRANSPORT PROTEIN Compound Transient receptor potential cation channel subfamily V member 1 Source (DKTX_HAPSC) Sequence B:  TPLALAASSGKIGVLAYILQREIHEPECRHLSRKFTEWAY GPVHSSLYDLSCIDTCEKNSVLEVIAYSSSETPNRHDMLL VEPLNRLLQDKWDRFVKRIFYFNFFVYCLYMIIFTAAAYY RPVEGLPPYKLKNTVGDYFRVTGEILSVSGGVYFFFRGIQ YFLQRRPSLKSLFVDSYSEILFFVQSLFMLVSVVLYFSQR KEYVASMVFSLAMGWTNMLYYTRGFQQMGIYAVMIEKMIL RDLCRFMFVYLVFLFGFSTAVVTLIEDGKYNSLYSTCLEL FKFTIGMGDLEFTENYDFKAVFIILLLAYVILTYILLLNM LIALMGETVNKIAQESKNIWKLQRAITILDTEKSFLKCMR KAFRSGKLLQVGFTPDGKDDYRWCFRVDEVNWTT Description (1)  Transient receptor potential cation channel subfamily V member 1, Tau-theraphotoxin-Hs1a Functional site 1) chain B residue 591 type sequence F description binding site for residue 6EU A 804 source : AC4 2) chain B residue 668 type sequence I description binding site for residue 6EU A 804 source : AC4 3) chain B residue 669 type sequence L description binding site for residue 6EU A 804 source : AC4 4) chain B residue 437 type sequence N description binding site for residue 6O8 B 801 source : AC5 5) chain B residue 440 type sequence V description binding site for residue 6O8 B 801 source : AC5 6) chain B residue 487 type sequence Y description binding site for residue 6O8 B 801 source : AC5 7) chain B residue 488 type sequence F description binding site for residue 6O8 B 801 source : AC5 8) chain B residue 491 type sequence R description binding site for residue 6O8 B 801 source : AC5 9) chain B residue 513 type sequence E description binding site for residue 6O8 B 801 source : AC5 10) chain B residue 516 type sequence F description binding site for residue 6O8 B 801 source : AC5 11) chain B residue 554 type sequence Y description binding site for residue 6O8 B 801 source : AC5 12) chain B residue 555 type sequence Y description binding site for residue 6O8 B 801 source : AC5 13) chain B residue 532 type sequence S description binding site for residue 6OE B 802 source : AC6 14) chain B residue 534 type sequence R description binding site for residue 6OE B 802 source : AC6 15) chain B residue 511 type sequence Y description binding site for residue 6EU B 803 source : AC7 16) chain B residue 512 type sequence S description binding site for residue 6EU B 803 source : AC7 17) chain B residue 514 type sequence I description binding site for residue 6EU B 803 source : AC7 18) chain B residue 515 type sequence L description binding site for residue 6EU B 803 source : AC7 19) chain B residue 546 type sequence A description binding site for residue 6EU B 803 source : AC7 20) chain B residue 547 type sequence M description binding site for residue 6EU B 803 source : AC7 21) chain B residue 550 type sequence T description binding site for residue 6EU B 803 source : AC7 22) chain B residue 551 type sequence N description binding site for residue 6EU B 803 source : AC7 23) chain B residue 553 type sequence L description binding site for residue 6EU B 803 source : AC7 24) chain B residue 554 type sequence Y description binding site for residue 6EU B 803 source : AC7 25) chain B residue 557 type sequence R description binding site for residue 6EU B 803 source : AC7 26) chain B residue 566 type sequence A description binding site for residue 6EU B 803 source : AC7 27) chain B residue 569 type sequence I description binding site for residue 6EU B 803 source : AC7 28) chain B residue 573 type sequence I description binding site for residue 6EU B 803 source : AC7 29) chain B residue 453 type sequence Y description binding site for residue 6OE D 803 source : AD4 30) chain B residue 534 type sequence R description binding site for residue 6O9 F 101 source : AD9 31) chain B residue 629 type sequence S description binding site for residue 6OE F 103 source : AE2 32) chain B residue 631 type sequence Y description binding site for residue 6OE F 103 source : AE2 33) chain B residue 650-672 type INTRAMEM sequence TENYDFKAVFIILLLAYVILTYI description Pore-forming => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200, ECO:0000305|PubMed:10931826 source Swiss-Prot : SWS_FT_FI4 34) chain B residue 370 type MOD_RES sequence T description Phosphothreonine; by PKA; in vitro => ECO:0000269|PubMed:12194871 source Swiss-Prot : SWS_FT_FI10 35) chain B residue 502 type MOD_RES sequence S description Phosphoserine; by PKC/PRKCE => ECO:0000269|PubMed:11884385, ECO:0000269|PubMed:12194871, ECO:0000269|PubMed:14630912 source Swiss-Prot : SWS_FT_FI11 36) chain B residue 727 type MOD_RES sequence Q description Phosphothreonine => ECO:0000269|PubMed:14630912 source Swiss-Prot : SWS_FT_FI12 37) chain B residue 627 type CARBOHYD sequence Y description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11683872 source Swiss-Prot : SWS_FT_FI13 38) chain B residue 511 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 39) chain B residue 550 type BINDING sequence T description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 40) chain B residue 557 type BINDING sequence R description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX source Swiss-Prot : SWS_FT_FI7 41) chain B residue 669 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:Q9R186 source Swiss-Prot : SWS_FT_FI8 42) chain B residue 536-556 type TRANSMEM sequence EYVASMVFSLAMGWTNMLYYT description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI1 43) chain B residue 572-599 type TRANSMEM sequence MILRDLCRFMFVYLVFLFGFSTAVVTLI description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI1 44) chain B residue 681-709 type TRANSMEM sequence LMGETVNKIAQESKNIWKLQRAITILDTE description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI1 45) chain B residue 433-453 type TRANSMEM sequence IFYFNFFVYCLYMIIFTAAAY description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI1 46) chain B residue 472-497 type TRANSMEM sequence YFRVTGEILSVSGGVYFFFRGIQYFL description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI1 47) chain B residue 511-531 type TRANSMEM sequence YSEILFFVQSLFMLVSVVLYF description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI1 48) chain B residue 498-510 type TOPO_DOM sequence QRRPSLKSLFVDS description Cytoplasmic => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI3 49) chain B residue 557-571 type TOPO_DOM sequence RGFQQMGIYAVMIEK description Cytoplasmic => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI3 50) chain B residue 454-471 type TOPO_DOM sequence YRPVEGLPPYKLKNTVGD description Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI2 51) chain B residue 532-535 type TOPO_DOM sequence SQRK description Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI2 52) chain B residue 600-649 type TOPO_DOM sequence EDGKYNSLYSTCLELFKFTIGMGDLEF description Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200 source Swiss-Prot : SWS_FT_FI2

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